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Reviewed, UniProtKB/Swiss-Prot Q5P4A1 (LEXA_AZOSE)

Last modified November 3, 2009. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    LexA repressor
    EC=3.4.21.88
Gene names
Name: lexA
Ordered Locus Names: AZOSEA17370
ORF Names: ebA3086
OrganismAzoarcus sp. (strain EbN1) (Aromatoleum aromaticum (strain EbN1)) [Complete proteome] [HAMAP]
Taxonomic identifier76114 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeAromatoleum

Protein attributes

Sequence length203 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, recA interacts with lexA causing an autocatalytic cleavage which disrupts the DNA-binding part of lexA, leading to derepression of the SOS regulon and eventually DNA repair By similarity.

Catalytic activity

Hydrolysis of Ala-|-Gly bond in repressor lexA. HAMAP MF_00015

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the peptidase S24 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 203203LexA repressor HAMAP MF_00015
PRO_0000170001

Regions

DNA binding32 – 5221H-T-H motif By similarity

Sites

Active site1211For autocatalytic cleavage activity By similarity
Active site1581For autocatalytic cleavage activity By similarity
Site86 – 872Cleavage; by autolysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5P4A1-1 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 802F1EE3FF9BCE90

FASTA20322,207
        10         20         30         40         50         60 
MISRADPLTA RQAEILDFIR HTVESEGRPP TRAEICTAFG FRSPNAAETH LRTLAAKGAI 

        70         80         90        100        110        120 
VLEEGRARGI RLVEALGLPL VGHVAAGRPM LAVEHIEARY QIDSALFSPR ADYLLRVRGM 

       130        140        150        160        170        180 
SMRDAGIIDS DLLAVHRTPQ VRAGQVVVAR LEDEVTVKTF TREGPIVRLL PANPDFEPIV 

       190        200 
VDTRHQALDI EGIAVGLVRN GSR 

« Hide

References

[1]"The genome sequence of an anaerobic aromatic-degrading denitrifying bacterium, strain EbN1."
Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., Reinhardt R.
Arch. Microbiol. 183:27-36(2005) [PubMed: 15551059] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CR555306 Genomic DNA. Translation: CAI07862.1.
RefSeqYP_158763.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ5P4A1.

Protein family/group databases

MEROPSS24.001.

Genome annotation databases

GeneID3181911.
GenomeReviewsGene locus AZOSEA17370 in contig CR555306_GR.
KEGGeba:ebA3086.
NMPDRfig|76114.4.peg.960.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ5P4A1.
OMAKVIGVFR.

Enzyme and pathway databases

BioCycASP76114:EBA3086-MON.

Family and domain databases

HAMAPMF_00015.
[Tree]
InterProIPR006199. LexA_DNA_bd.
IPR006200. Pept_S24_LexA.
IPR006197. Peptidase_S24_LexA_cons-reg.
IPR019759. Peptidase_S24_S26_cons-reg.
IPR011056. Peptidase_S24_S26A/B/C_b-rbn.
IPR011991. Wing_hlx_DNA_bd.
[Graphical view]
Gene3DG3DSA:2.10.109.10. Pept_S24_S26_C. 1 hit.
G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
PfamPF01726. LexA_DNA_bind. 1 hit.
PF00717. Peptidase_S24. 1 hit.
[Graphical view]
PRINTSPR00726. LEXASERPTASE.
TIGRFAMsTIGR00498. lexA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLEXA_AZOSE
AccessionPrimary (citable) accession number: Q5P4A1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 2, 2005
Last sequence update: January 4, 2005
Last modified: November 3, 2009
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents